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Protein

Integrin alpha-IIb

Gene

ITGA2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi274 – 282Sequence analysis9
Calcium bindingi328 – 336Sequence analysis9
Calcium bindingi396 – 404Sequence analysis9
Calcium bindingi457 – 465Sequence analysis9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000005961-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLinkiP08514.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-IIb
Alternative name(s):
GPalpha IIb
Short name:
GPIIb
Platelet membrane glycoprotein IIb
CD_antigen: CD41
Cleaved into the following 3 chains:
Gene namesi
Name:ITGA2B
Synonyms:GP2B, ITGAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6138. ITGA2B.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 993ExtracellularSequence analysisAdd BLAST962
Transmembranei994 – 1019HelicalSequence analysisAdd BLAST26
Topological domaini1020 – 1039CytoplasmicSequence analysisAdd BLAST20

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • integrin complex Source: InterPro
  • plasma membrane Source: Reactome
  • platelet alpha granule membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Glanzmann thrombasthenia (GT)20 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
See also OMIM:273800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03044586L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication1
Natural variantiVAR_030446139A → V in GT. 1 Publication1
Natural variantiVAR_030447161C → W in GT. 1 Publication1
Natural variantiVAR_030448174Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication1
Natural variantiVAR_009885176P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications1
Natural variantiVAR_009886176P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication1
Natural variantiVAR_030449202F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication1
Natural variantiVAR_030450207T → I in GT. 1 Publication1
Natural variantiVAR_030451214L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 PublicationCorresponds to variant rs137852911dbSNPEnsembl.1
Natural variantiVAR_030452222F → L in GT. 1 Publication1
Natural variantiVAR_030453267G → E in GT. 1 Publication1
Natural variantiVAR_003979273G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 PublicationCorresponds to variant rs137852907dbSNPEnsembl.1
Natural variantiVAR_009887320F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication1
Natural variantiVAR_030454329V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication1
Natural variantiVAR_009888355E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 PublicationsCorresponds to variant rs137852910dbSNPEnsembl.1
Natural variantiVAR_003980358R → H in GT; type II. 1 PublicationCorresponds to variant rs137852908dbSNPEnsembl.1
Natural variantiVAR_030455380G → D in GT. 1 PublicationCorresponds to variant rs766006685dbSNPEnsembl.1
Natural variantiVAR_030456405I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 PublicationsCorresponds to variant rs75622274dbSNPEnsembl.1
Natural variantiVAR_030457412G → R in GT. 1 PublicationCorresponds to variant rs780786843dbSNPEnsembl.1
Natural variantiVAR_003981449G → D in GT; type I. 1 Publication1
Natural variantiVAR_030458456 – 457Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface. 2
Natural variantiVAR_030459581A → D in GT. 1 Publication1
Natural variantiVAR_030460596I → T in GT; type I. 3 PublicationsCorresponds to variant rs76811038dbSNPEnsembl.1
Natural variantiVAR_030461705C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 PublicationsCorresponds to variant rs77961246dbSNPEnsembl.1
Natural variantiVAR_030462752L → V in GT. 1 PublicationCorresponds to variant rs761174160dbSNPEnsembl.1
Natural variantiVAR_030463755R → P in GT. 1 PublicationCorresponds to variant rs763762304dbSNPEnsembl.1
Natural variantiVAR_003982778Q → P in GT; type II. 3 PublicationsCorresponds to variant rs74475415dbSNPEnsembl.1
Natural variantiVAR_030464847L → P in GT. 1 Publication1
Natural variantiVAR_069917934V → F in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 PublicationCorresponds to variant rs77458039dbSNPEnsembl.1
Natural variantiVAR_030465943P → L in GT; marked reduction in the rate of surface expression. 1 Publication1
Natural variantiVAR_069918957S → L in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein. 1 PublicationCorresponds to variant rs80002943dbSNPEnsembl.1
Natural variantiVAR_030466982V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 PublicationsCorresponds to variant rs78657866dbSNPEnsembl.1
Natural variantiVAR_0304681026R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications1
Bleeding disorder, platelet-type 16 (BDPLT16)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities.
See also OMIM:187800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0304681026R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications1
Natural variantiVAR_0699191026R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1029 – 1030PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3674.
MalaCardsiITGA2B.
MIMi187800. phenotype.
273800. phenotype.
OpenTargetsiENSG00000005961.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA29938.

Chemistry databases

ChEMBLiCHEMBL212.
DrugBankiDB00054. Abciximab.
DB00775. Tirofiban.

Polymorphism and mutation databases

BioMutaiITGA2B.
DMDMi226694183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 313 PublicationsAdd BLAST31
ChainiPRO_000001627532 – 1039Integrin alpha-IIbAdd BLAST1008
ChainiPRO_000001627632 – 887Integrin alpha-IIb heavy chainAdd BLAST856
ChainiPRO_0000292348891 – 1039Integrin alpha-IIb light chain, form 1Add BLAST149
ChainiPRO_0000016277903 – 1039Integrin alpha-IIb light chain, form 2Add BLAST137

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...)1 Publication1
Disulfide bondi87 ↔ 961 Publication
Disulfide bondi138 ↔ 1611 Publication
Disulfide bondi177 ↔ 1981 Publication
Glycosylationi280N-linked (GlcNAc...)1 Publication1
Disulfide bondi504 ↔ 5151 Publication
Disulfide bondi521 ↔ 5761 Publication
Glycosylationi601N-linked (GlcNAc...)2 Publications1
Disulfide bondi633 ↔ 6391 Publication
Disulfide bondi705 ↔ 7181 Publication
Glycosylationi711N-linked (GlcNAc...)1 Publication1
Disulfide bondi857 ↔ 911Interchain (between heavy and light chains)1 Publication
Glycosylationi874O-linked (GalNAc...); in alloantigen HPA-3B1
Glycosylationi878O-linked (GalNAc...)1 Publication1
Modified residuei891Pyrrolidone carboxylic acid; in light chain form 11 Publication1
Disulfide bondi916 ↔ 9211 Publication
Glycosylationi962N-linked (GlcNAc...)1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP08514.
PeptideAtlasiP08514.
PRIDEiP08514.
TopDownProteomicsiP08514-1. [P08514-1]

2D gel databases

OGPiP08514.

PTM databases

iPTMnetiP08514.
PhosphoSitePlusiP08514.

Miscellaneous databases

PMAP-CutDBQ17R67.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

Gene expression databases

BgeeiENSG00000005961.
CleanExiHS_ITGA2B.
ExpressionAtlasiP08514. baseline and differential.
GenevisibleiP08514. HS.

Organism-specific databases

HPAiCAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-702693,EBI-702693
ITGB3P0510611EBI-702693,EBI-702847

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi109881. 11 interactors.
DIPiDIP-68N.
IntActiP08514. 2 interactors.
STRINGi9606.ENSP00000262407.

Chemistry databases

BindingDBiP08514.

Structurei

Secondary structure

11039
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi52 – 58Combined sources7
Beta strandi60 – 62Combined sources3
Beta strandi64 – 70Combined sources7
Beta strandi78 – 80Combined sources3
Beta strandi82 – 88Combined sources7
Beta strandi93 – 95Combined sources3
Beta strandi107 – 110Combined sources4
Beta strandi113 – 118Combined sources6
Beta strandi126 – 131Combined sources6
Beta strandi134 – 139Combined sources6
Beta strandi143 – 148Combined sources6
Beta strandi151 – 153Combined sources3
Beta strandi160 – 164Combined sources5
Turni166 – 168Combined sources3
Beta strandi171 – 174Combined sources4
Helixi183 – 188Combined sources6
Turni189 – 193Combined sources5
Beta strandi202 – 206Combined sources5
Beta strandi211 – 216Combined sources6
Helixi219 – 222Combined sources4
Beta strandi225 – 230Combined sources6
Helixi231 – 237Combined sources7
Helixi259 – 261Combined sources3
Beta strandi268 – 273Combined sources6
Beta strandi279 – 281Combined sources3
Beta strandi283 – 288Combined sources6
Helixi291 – 294Combined sources4
Beta strandi297 – 301Combined sources5
Beta strandi307 – 312Combined sources6
Beta strandi324 – 327Combined sources4
Beta strandi330 – 333Combined sources4
Beta strandi336 – 341Combined sources6
Beta strandi345 – 348Combined sources4
Turni349 – 351Combined sources3
Beta strandi352 – 355Combined sources4
Beta strandi358 – 362Combined sources5
Beta strandi366 – 368Combined sources3
Beta strandi375 – 379Combined sources5
Beta strandi391 – 395Combined sources5
Beta strandi400 – 402Combined sources3
Beta strandi404 – 409Combined sources6
Beta strandi413 – 417Combined sources5
Beta strandi419 – 423Combined sources5
Beta strandi427 – 430Combined sources4
Beta strandi435 – 439Combined sources5
Beta strandi450 – 456Combined sources7
Beta strandi458 – 463Combined sources6
Beta strandi465 – 470Combined sources6
Helixi471 – 473Combined sources3
Beta strandi475 – 479Combined sources5
Beta strandi484 – 493Combined sources10
Beta strandi507 – 509Combined sources3
Beta strandi512 – 525Combined sources14
Beta strandi534 – 541Combined sources8
Turni542 – 544Combined sources3
Helixi547 – 549Combined sources3
Beta strandi551 – 554Combined sources4
Turni555 – 557Combined sources3
Beta strandi559 – 567Combined sources9
Beta strandi575 – 583Combined sources9
Helixi586 – 588Combined sources3
Beta strandi596 – 603Combined sources8
Beta strandi616 – 619Combined sources4
Beta strandi622 – 627Combined sources6
Turni634 – 637Combined sources4
Beta strandi643 – 651Combined sources9
Beta strandi653 – 655Combined sources3
Beta strandi662 – 670Combined sources9
Beta strandi678 – 683Combined sources6
Beta strandi688 – 695Combined sources8
Beta strandi705 – 708Combined sources4
Beta strandi710 – 713Combined sources4
Beta strandi715 – 721Combined sources7
Beta strandi728 – 738Combined sources11
Beta strandi746 – 755Combined sources10
Beta strandi759 – 761Combined sources3
Beta strandi767 – 774Combined sources8
Beta strandi779 – 792Combined sources14
Beta strandi810 – 819Combined sources10
Beta strandi821 – 823Combined sources3
Beta strandi825 – 836Combined sources12
Beta strandi842 – 854Combined sources13
Beta strandi856 – 861Combined sources6
Beta strandi906 – 909Combined sources4
Turni911 – 913Combined sources3
Beta strandi916 – 926Combined sources11
Beta strandi931 – 940Combined sources10
Helixi942 – 945Combined sources4
Beta strandi952 – 965Combined sources14
Beta strandi967 – 969Combined sources3
Beta strandi977 – 988Combined sources12
Turni991 – 994Combined sources4
Helixi997 – 1020Combined sources24
Beta strandi1022 – 1024Combined sources3
Turni1025 – 1027Combined sources3
Helixi1028 – 1031Combined sources4
Turni1035 – 1038Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2MTPNMR-B1019-1039[»]
2N9YNMR-A989-1029[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
4Z7NX-ray2.60A/C32-486[»]
4Z7OX-ray2.85A/C32-486[»]
4Z7QX-ray2.70A/C32-485[»]
5HDBX-ray2.70A/C32-485[»]
ProteinModelPortaliP08514.
SMRiP08514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati35 – 96FG-GAP 1PROSITE-ProRule annotationAdd BLAST62
Repeati110 – 173FG-GAP 2PROSITE-ProRule annotationAdd BLAST64
Repeati187 – 238FG-GAP 3PROSITE-ProRule annotationAdd BLAST52
Repeati251 – 305FG-GAP 4PROSITE-ProRule annotationAdd BLAST55
Repeati306 – 371FG-GAP 5PROSITE-ProRule annotationAdd BLAST66
Repeati373 – 432FG-GAP 6PROSITE-ProRule annotationAdd BLAST60
Repeati435 – 496FG-GAP 7PROSITE-ProRule annotationAdd BLAST62

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1022 – 1026GFFKR motif5

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08514.
KOiK06476.
OMAiLWLLEWV.
OrthoDBiEOG091G05Z4.
PhylomeDBiP08514.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08514-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF
60 70 80 90 100
GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL
110 120 130 140 150
FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT
160 170 180 190 200
EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA
210 220 230 240 250
GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ
260 270 280 290 300
SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI
310 320 330 340 350
LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD
360 370 380 390 400
RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD
410 420 430 440 450
GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF
460 470 480 490 500
SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA
510 520 530 540 550
VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR
560 570 580 590 600
RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL
610 620 630 640 650
NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT
660 670 680 690 700
GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF
710 720 730 740 750
ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF
760 770 780 790 800
QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE
810 820 830 840 850
QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ
860 870 880 890 900
PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP
910 920 930 940 950
SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL
960 970 980 990 1000
DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV
1010 1020 1030
LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE
Length:1,039
Mass (Da):113,377
Last modified:April 14, 2009 - v3
Checksum:i063EE298E026F116
GO
Isoform 2 (identifier: P08514-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     948-981: Missing.

Show »
Length:1,005
Mass (Da):109,574
Checksum:i81C09F0D904CB534
GO
Isoform 3 (identifier: P08514-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

Show »
Length:953
Mass (Da):103,218
Checksum:i0100D4C5919320BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23P → A in AAA35926 (PubMed:2345548).Curated1
Sequence conflicti120A → S in BAG37735 (PubMed:14702039).Curated1
Sequence conflicti287 – 288GA → VP in AAA53150 (PubMed:2322558).Curated2
Sequence conflicti346E → D in AAA35926 (PubMed:2345548).Curated1
Sequence conflicti565N → D in AAA35926 (PubMed:2345548).Curated1
Sequence conflicti566L → V in CAA29987 (PubMed:3422188).Curated1
Sequence conflicti633C → S in AAA60114 (PubMed:2439501).Curated1
Sequence conflicti729Q → E in CAA29987 (PubMed:3422188).Curated1
Sequence conflicti971P → A in AAA53150 (PubMed:2322558).Curated1
Sequence conflicti1029P → H in AAA35926 (PubMed:2345548).Curated1
Sequence conflicti1029P → H in AAA52588 (PubMed:2845986).Curated1
Sequence conflicti1030P → T in AAA52588 (PubMed:2845986).Curated1

Polymorphismi

Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01417640T → I.1 PublicationCorresponds to variant rs5915dbSNPEnsembl.1
Natural variantiVAR_03044586L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication1
Natural variantiVAR_030446139A → V in GT. 1 Publication1
Natural variantiVAR_030447161C → W in GT. 1 Publication1
Natural variantiVAR_030448174Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication1
Natural variantiVAR_009885176P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications1
Natural variantiVAR_009886176P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication1
Natural variantiVAR_030449202F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication1
Natural variantiVAR_030450207T → I in GT. 1 Publication1
Natural variantiVAR_030451214L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 PublicationCorresponds to variant rs137852911dbSNPEnsembl.1
Natural variantiVAR_030452222F → L in GT. 1 Publication1
Natural variantiVAR_030453267G → E in GT. 1 Publication1
Natural variantiVAR_003979273G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 PublicationCorresponds to variant rs137852907dbSNPEnsembl.1
Natural variantiVAR_054820313G → A.2 PublicationsCorresponds to variant rs1126554dbSNPEnsembl.1
Natural variantiVAR_009887320F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication1
Natural variantiVAR_030454329V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication1
Natural variantiVAR_009888355E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 PublicationsCorresponds to variant rs137852910dbSNPEnsembl.1
Natural variantiVAR_003980358R → H in GT; type II. 1 PublicationCorresponds to variant rs137852908dbSNPEnsembl.1
Natural variantiVAR_030455380G → D in GT. 1 PublicationCorresponds to variant rs766006685dbSNPEnsembl.1
Natural variantiVAR_030456405I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 PublicationsCorresponds to variant rs75622274dbSNPEnsembl.1
Natural variantiVAR_030457412G → R in GT. 1 PublicationCorresponds to variant rs780786843dbSNPEnsembl.1
Natural variantiVAR_003981449G → D in GT; type I. 1 Publication1
Natural variantiVAR_030458456 – 457Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface. 2
Natural variantiVAR_030459581A → D in GT. 1 Publication1
Natural variantiVAR_030460596I → T in GT; type I. 3 PublicationsCorresponds to variant rs76811038dbSNPEnsembl.1
Natural variantiVAR_054821649V → L.Corresponds to variant rs7207402dbSNPEnsembl.1
Natural variantiVAR_030461705C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 PublicationsCorresponds to variant rs77961246dbSNPEnsembl.1
Natural variantiVAR_030462752L → V in GT. 1 PublicationCorresponds to variant rs761174160dbSNPEnsembl.1
Natural variantiVAR_030463755R → P in GT. 1 PublicationCorresponds to variant rs763762304dbSNPEnsembl.1
Natural variantiVAR_003982778Q → P in GT; type II. 3 PublicationsCorresponds to variant rs74475415dbSNPEnsembl.1
Natural variantiVAR_030464847L → P in GT. 1 Publication1
Natural variantiVAR_003983874I → S Alloantigen HPA-3B. 1 PublicationCorresponds to variant rs5911dbSNPEnsembl.1
Natural variantiVAR_069917934V → F in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 PublicationCorresponds to variant rs77458039dbSNPEnsembl.1
Natural variantiVAR_030465943P → L in GT; marked reduction in the rate of surface expression. 1 Publication1
Natural variantiVAR_069918957S → L in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein. 1 PublicationCorresponds to variant rs80002943dbSNPEnsembl.1
Natural variantiVAR_014177968Y → N.1 PublicationCorresponds to variant rs5914dbSNPEnsembl.1
Natural variantiVAR_030466982V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 PublicationsCorresponds to variant rs78657866dbSNPEnsembl.1
Natural variantiVAR_030467989A → T.2 PublicationsCorresponds to variant rs78165611dbSNPEnsembl.1
Natural variantiVAR_0304681026R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications1
Natural variantiVAR_0699191026R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002736910 – 1039SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3. CuratedAdd BLAST130
Alternative sequenceiVSP_002737948 – 981Missing in isoform 2. CuratedAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSiCCDS32665.1. [P08514-1]
PIRiA34269.
RefSeqiNP_000410.2. NM_000419.4. [P08514-1]
XP_011523051.1. XM_011524749.1. [P08514-2]
UniGeneiHs.411312.

Genome annotation databases

EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
GeneIDi3674.
KEGGihsa:3674.
UCSCiuc002igt.2. human. [P08514-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSiCCDS32665.1. [P08514-1]
PIRiA34269.
RefSeqiNP_000410.2. NM_000419.4. [P08514-1]
XP_011523051.1. XM_011524749.1. [P08514-2]
UniGeneiHs.411312.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2MTPNMR-B1019-1039[»]
2N9YNMR-A989-1029[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
4Z7NX-ray2.60A/C32-486[»]
4Z7OX-ray2.85A/C32-486[»]
4Z7QX-ray2.70A/C32-485[»]
5HDBX-ray2.70A/C32-485[»]
ProteinModelPortaliP08514.
SMRiP08514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109881. 11 interactors.
DIPiDIP-68N.
IntActiP08514. 2 interactors.
STRINGi9606.ENSP00000262407.

Chemistry databases

BindingDBiP08514.
ChEMBLiCHEMBL212.
DrugBankiDB00054. Abciximab.
DB00775. Tirofiban.

PTM databases

iPTMnetiP08514.
PhosphoSitePlusiP08514.

Polymorphism and mutation databases

BioMutaiITGA2B.
DMDMi226694183.

2D gel databases

OGPiP08514.

Proteomic databases

PaxDbiP08514.
PeptideAtlasiP08514.
PRIDEiP08514.
TopDownProteomicsiP08514-1. [P08514-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
GeneIDi3674.
KEGGihsa:3674.
UCSCiuc002igt.2. human. [P08514-1]

Organism-specific databases

CTDi3674.
DisGeNETi3674.
GeneCardsiITGA2B.
HGNCiHGNC:6138. ITGA2B.
HPAiCAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.
MalaCardsiITGA2B.
MIMi187800. phenotype.
273800. phenotype.
607759. gene.
neXtProtiNX_P08514.
OpenTargetsiENSG00000005961.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA29938.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08514.
KOiK06476.
OMAiLWLLEWV.
OrthoDBiEOG091G05Z4.
PhylomeDBiP08514.
TreeFamiTF105391.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000005961-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLinkiP08514.

Miscellaneous databases

ChiTaRSiITGA2B. human.
EvolutionaryTraceiP08514.
GeneWikiiITGA2B.
GenomeRNAii3674.
PMAP-CutDBQ17R67.
PROiP08514.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005961.
CleanExiHS_ITGA2B.
ExpressionAtlasiP08514. baseline and differential.
GenevisibleiP08514. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITA2B_HUMAN
AccessioniPrimary (citable) accession number: P08514
Secondary accession number(s): B2RCY8
, O95366, Q14443, Q17R67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 14, 2009
Last modified: November 30, 2016
This is version 212 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.